This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1bhg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1bhg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhg, resolution 2.53&Aring;" /> '''HUMAN BETA-GLUCURON...)
Next diff →

Revision as of 14:03, 12 November 2007


1bhg, resolution 2.53Å

Drag the structure with the mouse to rotate

HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION

Contents

Overview

The X-ray structure of the homotetrameric lysosomal acid hydrolase, human, beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution., The tetramer has approximate dihedral symmetry and each promoter consists, of three structural domains with topologies similar to a jelly roll, barrel, an immunoglobulin constant domain and a TIM barrel respectively., Residues 179-204 form a beta-hairpin motif similar to the putative, lysosomal targeting motif of cathepsin D, supporting the view that, lysosomal targeting has a structural basis. The active site of the enzyme, is formed from a large cleft at the interface of two monomers. Residues, Glu 451 and Glu 540 are proposed to be important for catalysis. The, structure establishes a framework for understanding mutations that lead to, the human genetic disease mucopolysaccharidosis VII, and for using the, enzyme in anti-cancer therapy.

Disease

Known disease associated with this structure: Mucopolysaccharidosis VII OMIM:[253220]

About this Structure

1BHG is a Single protein structure of sequence from Homo sapiens. Active as Beta-glucuronidase, with EC number 3.2.1.31 Full crystallographic information is available from OCA.

Reference

Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs., Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH, Nat Struct Biol. 1996 Apr;3(4):375-81. PMID:8599764

Page seeded by OCA on Mon Nov 12 16:09:45 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools